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1PIN

PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0001666biological_processresponse to hypoxia
A0001932biological_processregulation of protein phosphorylation
A0001934biological_processpositive regulation of protein phosphorylation
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0003774molecular_functioncytoskeletal motor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007049biological_processcell cycle
A0007088biological_processregulation of mitotic nuclear division
A0008013molecular_functionbeta-catenin binding
A0010468biological_processregulation of gene expression
A0016607cellular_componentnuclear speck
A0016853molecular_functionisomerase activity
A0016859molecular_functioncis-trans isomerase activity
A0030182biological_processneuron differentiation
A0030496cellular_componentmidbody
A0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
A0031434molecular_functionmitogen-activated protein kinase kinase binding
A0031647biological_processregulation of protein stability
A0032091biological_processnegative regulation of protein binding
A0032092biological_processpositive regulation of protein binding
A0032465biological_processregulation of cytokinesis
A0032794molecular_functionGTPase activating protein binding
A0035307biological_processpositive regulation of protein dephosphorylation
A0036064cellular_componentciliary basal body
A0042177biological_processnegative regulation of protein catabolic process
A0043547biological_processpositive regulation of GTPase activity
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046785biological_processmicrotubule polymerization
A0048156molecular_functiontau protein binding
A0050808biological_processsynapse organization
A0050815molecular_functionphosphoserine residue binding
A0050816molecular_functionphosphothreonine residue binding
A0050821biological_processprotein stabilization
A0051171biological_processobsolete regulation of nitrogen compound metabolic process
A0051219molecular_functionphosphoprotein binding
A0060255biological_processregulation of macromolecule metabolic process
A0060392biological_processnegative regulation of SMAD protein signal transduction
A0070373biological_processnegative regulation of ERK1 and ERK2 cascade
A0080090biological_processregulation of primary metabolic process
A0090263biological_processpositive regulation of canonical Wnt signaling pathway
A0098978cellular_componentglutamatergic synapse
A0099524cellular_componentpostsynaptic cytosol
A1900180biological_processregulation of protein localization to nucleus
A1902430biological_processnegative regulation of amyloid-beta formation
A1990757molecular_functionubiquitin ligase activator activity
A2000146biological_processnegative regulation of cell motility
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ALA A 201
ChainResidue
APRO202
AHOH1113

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PRO A 202
ChainResidue
AHOH1141
AHOH1142
ALEU122
AGLN129
AMET130
AALA201

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
ALYS63
AARG68
AARG69
ASER154
AHOH1113

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 1PG A 300
ChainResidue
ATYR23
ASER32
AGLN33
ATRP34
ALYS97
AHOH1020
AHOH1036
AHOH1116
AHOH1163

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE 1PG A 301
ChainResidue
AHOH1198

site_idACT
Number of Residues3
DetailsTHE ACTIVE SITE OF THE PPIASE DOMAIN IS MARKED BY THE BOUND ALA-PRO DIPEPTIDE (CHAIN B).
ChainResidue
AHIS59
ACYS113
AHIS157

Functional Information from PROSITE/UniProt
site_idPS01096
Number of Residues21
DetailsPPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FEsLAsqfSdcs.Saka..RGdLG
ChainResidueDetails
APHE103-GLY123

site_idPS01159
Number of Residues27
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. WekrmsrssgrvYYfnhitnaSQWERP
ChainResidueDetails
ATRP11-PRO37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER43

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS46

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by DAPK1 => ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:29686383
ChainResidueDetails
ASER71

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
ASER108

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 511
ChainResidueDetails
AHIS59proton shuttle (general acid/base)
ACYS113covalently attached, electrostatic stabiliser
AGLN131electrostatic stabiliser
ASER154electrostatic stabiliser
AHIS157electrostatic stabiliser

218853

PDB entries from 2024-04-24

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